ID VPE_SOYBN Reviewed; 495 AA.
AC P49045;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Vacuolar-processing enzyme;
DE Short=VPE;
DE EC=3.4.22.-;
DE Flags: Precursor;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed cotyledon;
RX PubMed=8075902; DOI=10.1093/oxfordjournals.pcp.a078648;
RA Shimada T., Hiraiwa N., Nishimura M., Hara-Nishimura I.;
RT "Vacuolar processing enzyme of soybean that converts proproteins to the
RT corresponding mature forms.";
RL Plant Cell Physiol. 35:713-718(1994).
CC -!- FUNCTION: Asparagine-specific endopeptidase involved in the processing
CC of vacuolar seed protein precursors into the mature forms.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; D28876; BAA06030.1; -; mRNA.
DR PIR; T07132; T07132.
DR RefSeq; NP_001236678.1; NM_001249749.1.
DR AlphaFoldDB; P49045; -.
DR SMR; P49045; -.
DR STRING; 3847.P49045; -.
DR MEROPS; C13.001; -.
DR PaxDb; 3847-GLYMA17G14680-1; -.
DR GeneID; 547964; -.
DR KEGG; gmx:547964; -.
DR eggNOG; KOG1348; Eukaryota.
DR InParanoid; P49045; -.
DR OrthoDB; 2951493at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
DR CDD; cd21115; legumain_C; 1.
DR Gene3D; 1.10.132.130; -; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR043577; AE.
DR InterPro; IPR048501; Legum_prodom.
DR InterPro; IPR046427; Legumain_prodom_sf.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR12000:SF54; VACUOLAR-PROCESSING ENZYME BETA-ISOZYME; 1.
DR Pfam; PF20985; Legum_prodom; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500139; AE; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..495
FT /note="Vacuolar-processing enzyme"
FT /id="PRO_0000026524"
FT ACT_SITE 178
FT /evidence="ECO:0000250|UniProtKB:O89017"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O89017"
FT SITE 267
FT /note="Required for post-translational maturation and
FT enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q84LM2"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 253..267
FT /evidence="ECO:0000250|UniProtKB:P49046"
FT DISULFID 431..461
FT /evidence="ECO:0000250|UniProtKB:P49046"
FT DISULFID 443..478
FT /evidence="ECO:0000250|UniProtKB:P49046"
SQ SEQUENCE 495 AA; 55164 MW; 27FADB0D2B791F61 CRC64;
MALDRSIISK TTWYSVVLWM MVVLVRVHGA AARPNRKEWD SVIKLPTEPV DADSDEVGTR
WAVLVAGSNG YGNYRHQADV CHAYQLLIKG GLKEENIVVF MYDDIATNEL NPRHGVIINH
PEGEDLYAGV PKDYTGDNVT TENLFAVILG DKSKLKGGSG KVINSKPEDR IFIYYSDHGG
PGILGMPNMP YLYAMDFIDV LKKKHASGSY KEMVIYVEAC ESGSVFEGIM PKDLNIYVTT
ASNAQENSWG TYCPGMDPSP PPEYITCLGD LYSVAWMEDS EAHNLKRESV KQQYKSVKQR
TSNFNNYAMG SHVMQYGDTN ITAEKLYLYQ GFDPATVNFP PQNGRLETKM EVVNQRDAEL
FLLWQMYQRS NHQSENKTDI LKQIAETVKH RKHIDGSVEL IGVLLYGPGK GSSVLQSVRA
PGSSLVDDWT CLKSMVRVFE THCGTLTQYG MKHMRAFANI CNSGVSEASM EEACLAACEG
YNAGLFHPSN RGYSA
//
